Abstract

We have purified and characterized the cerebral amyloid protein that forms the plaque core in Alzheimer disease and in aged individuals with Down syndrome. The protein consists of multimeric aggregates of a polypeptide of about 40 residues (4 kDa). The amino acid composition, molecular mass, and NH2-terminal sequence of this amyloid protein are almost identical to those described for the amyloid deposited in the congophilic angiopathy of Alzheimer disease and Down syndrome, but the plaque core proteins have ragged NH2 termini. The shared 4-kDa subunit indicates a common origin for the amyloids of the plaque core and of the congophilic angiopathy. There are superficial resemblances between the solubility characteristics of the plaque core and some of the properties of scrapie infectivity, but there are no similarities in amino acid sequences between the plaque core and scrapie polypeptides.

Keywords

Amyloid (mycology)Protein subunitScrapieCerebral amyloid angiopathySenile plaquesAlzheimer's diseaseAngiopathyPeptide sequenceChemistryBiologyBiochemistryPathologyDiseaseMedicineDementiaPrion proteinEndocrinologyGene

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Publication Info

Year
1985
Type
article
Volume
82
Issue
12
Pages
4245-4249
Citations
4379
Access
Closed

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Colin L. Masters, G. Simms, Nicola A. Weinman et al. (1985). Amyloid plaque core protein in Alzheimer disease and Down syndrome.. Proceedings of the National Academy of Sciences , 82 (12) , 4245-4249. https://doi.org/10.1073/pnas.82.12.4245

Identifiers

DOI
10.1073/pnas.82.12.4245